The application of classical molecular
dynamics (MD) simulations
at atomic resolution (fine-grained level, FG), to most biomolecular
processes, remains limited because of the associated computational
complexity of representing all the atoms. This problem is magnified
in the presence of protein-based biomolecular systems that have a
very large conformational space, and MD simulations with fine-grained
resolution have slow dynamics to explore this space. Current transferable
coarse grained (CG) force fields in literature are either limited
to only peptides with the environment encoded in an implicit form
or cannot capture transitions into secondary/tertiary peptide structures
from a primary sequence of amino acids. In this work, we present a
transferable CG force field with an explicit representation of the
environment for accurate simulations with proteins. The force field
consists of a set of pseudoatoms representing different chemical groups
that can be joined/associated together to create different biomolecular
systems. This preserves the transferability of the force field to
multiple environments and simulation conditions. We have added electronic
polarization that can respond to environmental heterogeneity/fluctuations
and couple it to protein’s structural transitions. The nonbonded
interactions are parametrized with physics-based features such as
solvation and partitioning free energies determined by thermodynamic
calculations and matched with experiments and/or atomistic simulations.
The bonded potentials are inferred from corresponding distributions
in nonredundant protein structure databases. We present validations
of the CG model with simulations of well-studied aqueous protein systems
with specific protein fold typesTrp-cage, Trpzip4, villin,
WW-domain, and β-α-β. We also explore the applications
of the force field to study aqueous aggregation of Aβ 16-22
peptides.
Ionic liquids (ILs) are gaining attention as protein stabilizers and refolding additives. However, varying degrees of success with this approach motivates the need to better understand fundamental IL-protein interactions. A...
Scissoring/nonbuckling interconnects are proposed as a different route to stretchable structures, in which thick bar geometries replace thin ribbon layouts, to yield scissor‐like/nonbuckling deformations instead of in or out of plane buckling, as discussed in article number 1604989 by Shuodao Wang, John A. Rogers, and co‐authors. Metal and silicon structures with scissoring design can be stretched as much as 350% (previous maximum value 54%) and 90%, respectively, without fracture. Image designed by Zhenhai Li.
Long-term preservation of proteins at room temperature continues to be a major challenge. Towards using ionic liquids (ILs) to address this challenge, here we present a combination of experiments and...
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